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 25133

Title: HOXD13 Solution NMR Chemical Shift Coordinates   PubMed: 25491407

Deposition date: 2014-08-06 Original release date: 2022-05-12

Authors: Turner, Matthew; Ames, James

Citation: Turner, Matthew; Zhang, Yonghong; Carlson, Hanqian; Stadler, H Scott; Ames, James. "Chemical shift assignments of mouse HOXD13 DNA binding domain bound to duplex DNA"  Biomol. NMR Assign. 9, 267-270 (2015).

Assembly members:
HOXD13, polymer, 74 residues, Formula weight is not available

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):
HOXD13: GSHMLEGRKKRVPYTKLQLK ELENEYAINKFINKDKRRRI SAATNLSERQVTIWFQNRRV KDKKIVSKLKDTVS

Data sets:
Data typeCount
13C chemical shifts227
15N chemical shifts64
1H chemical shifts317

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HOXD131

Entities:

Entity 1, HOXD13 74 residues - Formula weight is not available

1   GLYSERHISMETLEUGLUGLYARGLYSLYS
2   ARGVALPROTYRTHRLYSLEUGLNLEULYS
3   GLULEUGLUASNGLUTYRALAILEASNLYS
4   PHEILEASNLYSASPLYSARGARGARGILE
5   SERALAALATHRASNLEUSERGLUARGGLN
6   VALTHRILETRPPHEGLNASNARGARGVAL
7   LYSASPLYSLYSILEVALSERLYSLEULYS
8   ASPTHRVALSER

Samples:

sample_1: HOXD13, [U-15N], 0.4 mM; H20 90%; D20 10%

sample_2: HOXD13, [U-13C;U-15N], 0.4 mM; H20 90%; D20 10%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 307 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH TOCSYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

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

NMR spectrometers:

  • Bruker Avance 800 MHz

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