BMRB Entry 16571

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16571

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

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).
PubMed: 20020226

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b+

Entity Sequences (FASTA):

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