BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15521

Title: Backbone Dynamics from 15N NMR Relaxation Measurements of the Rat Thyroid Transcription Factor 1 Homeodomain   PubMed: 18167145

Authors: Gumral, Devrim; Nadalin, Luana; Corazza, Alessandra; Fogolari, Federico; Damante, Giuseppe; Viglino, Paolo; Esposito, Gennaro

Citation: Gumral, Devrim; Nadalin, Luana; Corazza, Alessandra; Fogolari, Federico; Damante, Giuseppe; Viglino, Paolo; Esposito, Gennaro. "Helix mobility and recognition function of the rat thyroid transcription factor 1 homeodomain - hints from 15N-NMR relaxation studies"  FEBS J. 275, 435-448 (2007).

Assembly members:
TTF-1_HD, polymer, 68 residues, 8443.9 Da.

Natural source:   Common Name: rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

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

Entity Sequences (FASTA):
TTF-1_HD: MRRKRRVLFSQAQVYELERR FKQQKYLSAPEREHLASMIH LTPTQVKIWFQNHRYKMKRQ AKDKAAQQ

Data sets:
Data typeCount
15N chemical shifts86
1H chemical shifts101
heteronuclear NOE values66
T1 relaxation values66
T2 relaxation values66

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1TTF-1 HD1

Entities:

Entity 1, TTF-1 HD 68 residues - 8443.9 Da.

1   METARGARGLYSARGARGVALLEUPHESER
2   GLNALAGLNVALTYRGLULEUGLUARGARG
3   PHELYSGLNGLNLYSTYRLEUSERALAPRO
4   GLUARGGLUHISLEUALASERMETILEHIS
5   LEUTHRPROTHRGLNVALLYSILETRPPHE
6   GLNASNHISARGTYRLYSMETLYSARGGLN
7   ALALYSASPLYSALAALAGLNGLN

Samples:

sample_1: TTF-1 HD, [U-15N], 0.8 ± 0.1 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 4.3; pressure: 1 atm; temperature: 286 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N SQC-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N SQC-NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC based T1sample_1isotropicsample_conditions_1
2D 1H-15N HSQC based T2sample_1isotropicsample_conditions_1
2D 1H-15N HSQC based 1H-15N NOEsample_1isotropicsample_conditions_1

Software:

FELIX v97.0 (Accelrys), Accelrys Software Inc. - chemical shift assignment, data analysis, processing

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAA07231 BAA23527 BAA23529 BAB24155 BAB32434
EMBL CAA11493 CAA37851 CAA54868 CAA58053 CAG09890
GB AAA86099 AAA86100 AAA89066 AAB40921 AAB52381
PRF 2109233A 2109234A
REF NP_001003260 NP_001073136 NP_001079093 NP_001082031 NP_001089854
SP P23441 P43698 P43699 P50220 P97273
TPG DAA17483 DAA17484