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 15536

Title: Solution structure of Engrailed homeodomain WT   PubMed: 18274703

Authors: Religa, Tomasz

Citation: Religa, Tomasz. "Comparison of multiple crystal structures with NMR data for engrailed homeodomain"  J. Biomol. NMR 40, 189-202 (2008).

Assembly members:
EnHD, polymer, 61 residues, 7470.631 Da.

Natural source:   Common Name: fruit fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

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

Entity Sequences (FASTA):
EnHD: MDEKRPRTAFSSEQLARLKR EFNENRYLTERRRQQLSSEL GLNEAQIKIWFQNKRAKIKK S

Data sets:
Data typeCount
13C chemical shifts199
15N chemical shifts69
1H chemical shifts465
coupling constants45
order parameters58

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EnHD1

Entities:

Entity 1, EnHD 61 residues - 7470.631 Da.

1   METASPGLULYSARGPROARGTHRALAPHE
2   SERSERGLUGLNLEUALAARGLEULYSARG
3   GLUPHEASNGLUASNARGTYRLEUTHRGLU
4   ARGARGARGGLNGLNLEUSERSERGLULEU
5   GLYLEUASNGLUALAGLNILELYSILETRP
6   PHEGLNASNLYSARGALALYSILELYSLYS
7   SER

Samples:

U-15N: entity, [U-15N], 0.5 mM; d-sodium acetate 50 mM; sodium chloride 100 mM; H2O 93%; D2O 7%

U-D13C15N: entity, [U-13C; U-15N; ~70%-2H], 0.5 mM; d-sodium acetate 50 mM; sodium chloride 100 mM; H2O 93%; D2O 7%

278K: ionic strength: 145 mM; pH: 5.7; pressure: 1 atm; temperature: 278 K

298K: ionic strength: 145 mM; pH: 5.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYU-15Nisotropic278K
3D HNHAU-15Nisotropic278K
3D CBCA(CO)NHU-D13C15Nisotropic278K
Sidechain relaxation experimentsU-D13C15Nisotropic298K
Backbone relaxation experimentsU-D13C15Nisotropic298K

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

Tensor v2, Dosset, P.; Hus, J-C; Blackledge, M.; Marion - backbone dynamics data analysis

NMR spectrometers:

  • Bruker DRX500 500 MHz

Related Database Links:

PDB
SWS HMEN_DROME
BMRB 15520
DBJ BAN82729 BAN82730 BAN82731
EMBL CAA25906 CAA28436
GB AAA65478 AAF58639 AAL39593 AAM68711 ACL84189
PRF 1102248B
REF NP_523700 NP_725059 XP_001360552 XP_001958778 XP_001976053
SP P02836 P09145