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 15263

Title: 1H, 13C, and 15N Chemical Shift Assignments for NAB2 N-terminal domain   PubMed: 18190927

Authors: Grant, Richard; Marshall, Neil; Yang, Ji-Chun; Fasken, Milo; Kelly, Seth; Harreman, Michelle; Neuhaus, David; Corbett, Anita; Stewart, Murray

Citation: Grant, Richard; Marshall, Neil; Yang, Ji-Chun; Fasken, Milo; Kelly, Seth; Harreman, Michelle; Neuhaus, David; Corbett, Anita; Stewart, Murray. "Structure of the N-Terminal Mlp1-Binding Domain of the Saccharomyces cerevisiae mRNA-Binding Protein, Nab2"  J. Mol. Biol. 376, 1048-1059 (2008).

Assembly members:
NAB2_NTD, polymer, 105 residues, 11462.986 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
NAB2_NTD: MSQEQYTENLKVIVAEKLAG IPNFNEDIKYVAEYIVLLIV NGGTVESVVDELASLFDSVS RDTLANVVQTAFFALEALQQ GESAENIVSKIRMMNAQSLG QSDIA

Data sets:
Data typeCount
13C chemical shifts339
15N chemical shifts111
1H chemical shifts712

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NAB2 NTD polypeptide1

Entities:

Entity 1, NAB2 NTD polypeptide 105 residues - 11462.986 Da.

1   METSERGLNGLUGLNTYRTHRGLUASNLEU
2   LYSVALILEVALALAGLULYSLEUALAGLY
3   ILEPROASNPHEASNGLUASPILELYSTYR
4   VALALAGLUTYRILEVALLEULEUILEVAL
5   ASNGLYGLYTHRVALGLUSERVALVALASP
6   GLULEUALASERLEUPHEASPSERVALSER
7   ARGASPTHRLEUALAASNVALVALGLNTHR
8   ALAPHEPHEALALEUGLUALALEUGLNGLN
9   GLYGLUSERALAGLUASNILEVALSERLYS
10   ILEARGMETMETASNALAGLNSERLEUGLY
11   GLNSERASPILEALA

Samples:

sample_1: NAB2_NTD, [U-98% 13C; U-98% 15N], 2 mM; D2O, [U-2H], 10%; H2O 90%; sodium phosphate 25 mM; sodium chloride 10 mM

sample_conditions_1: ionic strength: 160 mM; pH: 6.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC CTsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESY 15N filtered in F2sample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAHBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

X-PLOR, Brunger - structure solution

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DMX 600 MHz
  • Bruker DRX 500 MHz

Related Database Links:

PDB
DBJ GAA23273
EMBL CAA96830 CAY79645
GB AAA34819 AAA34820 AAU09727 AHY79261 AJP38679
REF NP_011393
SP P32505
TPG DAA07987