BMRB Entry 16801

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16801
MolProbity Validation Chart

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Title:
Structure of residues 160-235 of putative peptidoglycan binding protein lmo0835 from Listeria monocytogenes: target LmR64B of the Northeast Structural Genomics Consortium
Deposition date:
2010-03-29
Original release date:
2012-08-03
Authors:
Cort, John; Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Cort, John. "Chemical shift assignments for fragment 160-235 of putative peptidoglycan bound protein lmo0835 from Listeria monocytogenes: target LmR64B of the Northeast Structural Genomics Consortium"  .

Assembly members:

Assembly members:
lmo0835, polymer, 85 residues, 9785.122 Da.

Natural source:

Natural source:   Common Name: Listeria monocytogenes   Taxonomy ID: 1639   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Listeria monocytogenes

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
lmo0835: MDFGKPNQVTVNYLDENNTS IAPSLYLSGLFNEAYNVPMK KIKGYTLLKYDSEILGVFTE SPQTINIIYQKKAPEQALEH HHHHH

Data sets:
Data typeCount
13C chemical shifts321
15N chemical shifts72
1H chemical shifts523

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1lmo08351

Entities:

Entity 1, lmo0835 85 residues - 9785.122 Da.

1   METASPPHEGLYLYSPROASNGLNVALTHR
2   VALASNTYRLEUASPGLUASNASNTHRSER
3   ILEALAPROSERLEUTYRLEUSERGLYLEU
4   PHEASNGLUALATYRASNVALPROMETLYS
5   LYSILELYSGLYTYRTHRLEULEULYSTYR
6   ASPSERGLUILELEUGLYVALPHETHRGLU
7   SERPROGLNTHRILEASNILEILETYRGLN
8   LYSLYSALAPROGLUGLNALALEUGLUHIS
9   HISHISHISHISHIS

Samples:

NC: lmo0835, [U-99% 13C; U-99% 15N], 0.92 mM; NaCl 100 mM; Sodium Acetate 20 mM; Calcium Chloride 5 mM; H2O 95%; D2O 5%

NC5: lmo0835, [5% 13C biosynthetically directed lableing, U-99% 15N], 0.92 mM; NaCl 100 mM; Sodium Acetate 20 mM; Calcium Chloride 5 mM; H2O 95%; D2O 5%

NC-D2O: lmo0835, [U-99% 13C; U-99% 15N], 0.92 mM; NaCl 100 mM; Sodium Acetate 20 mM; Calcium Chloride 5 mM; D2O 100%

sample_conditions_1: ionic strength: 125 mM; pH: 4.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQCNCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D HCCH-TOCSYNCisotropicsample_conditions_1
3D 1H-15N NOESYNCisotropicsample_conditions_1
3D 1H-13C NOESYNCisotropicsample_conditions_1
3D C(CO)NHNCisotropicsample_conditions_1
4D HCCH HMQC-NOESY-HMQCNC-D2Oisotropicsample_conditions_1
2D 1H-13C HSQCNC5isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
DBJ GAM91864 GAM94621
EMBL CAC98913 CAS04619 CBY03397 CBY48425 CBY51302
GB AAT03632 ABN80104 AEO05833 AEO25133 AEO38377
REF NP_464362 WP_003733401 WP_003743756 WP_009932757 WP_010958814

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