BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16571

Title: NMR assignments of the DNA binding domain of ML4 protein from Mesorhizobium loti   PubMed: 20020226

Deposition date: 2009-10-21 Original release date: 2010-01-28

Authors: Russo, Luigi; Palmieri, Maddalena; Baglivo, Ilaria; Esposito, Sabrina; Isernia, Carla; Malgieri, Gaetano; Pedone, Paolo V.

Citation: Russo, Luigi; Palmieri, Maddalena; Baglivo, Ilaria; Esposito, Sabrina; Isernia, Carla; Malgieri, Gaetano; Pedone, Paolo; Fattorusso, Roberto. "NMR assignments of the DNA binding domain of Ml4 protein from Mesorhizobium loti."  Biomol. NMR Assignments 4, 55-57 (2010).

Assembly members:
ML4, polymer, 100 residues, Formula weight is not available

Natural source:   Common Name: Mesorhizobium loti   Taxonomy ID: 381   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Mesorhizobium loti

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

Entity Sequences (FASTA):
ML4: GRPAEPENPVLTPAVNPKKS VFPDYIVSLEDGRKFKSMKR HLGLLGMTPDEYRTKWDLPR DYPMVAPNYAATRSALAKAS GLGRKAAPVKKAPAKRKAKA

Data sets:
Data typeCount
13C chemical shifts414
15N chemical shifts93
1H chemical shifts562

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ML41

Entities:

Entity 1, ML4 100 residues - Formula weight is not available

1   GLYARGPROALAGLUPROGLUASNPROVAL
2   LEUTHRPROALAVALASNPROLYSLYSSER
3   VALPHEPROASPTYRILEVALSERLEUGLU
4   ASPGLYARGLYSPHELYSSERMETLYSARG
5   HISLEUGLYLEULEUGLYMETTHRPROASP
6   GLUTYRARGTHRLYSTRPASPLEUPROARG
7   ASPTYRPROMETVALALAPROASNTYRALA
8   ALATHRARGSERALALEUALALYSALASER
9   GLYLEUGLYARGLYSALAALAPROVALLYS
10   LYSALAPROALALYSARGLYSALALYSALA

Samples:

sample_1: ML4, [U-100% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_2: ML4, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 10%; NaCl 0.2 M; phosphate buffer 20 mM

sample_conditions_1: ionic strength: 0.22 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_2isotropicsample_conditions_1
CBCGCDCEHEsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C TOCSYsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1

Software:

VNMR, Varian - collection

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Varian Unity INOVA 500 MHz

Related Database Links:

DBJ BAB51289
REF WP_010912631

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts