BMRB Entry 15377

Title:
Solution structure of human DESR1
Deposition date:
2007-07-12
Original release date:
2008-03-13
Authors:
Wu, Fangming; Wu, Jihui; Shi, Yunyu
Citation:

Citation: Wu, Fangming; Zhang, J.; Sun, J.; Huang, H.; Ji, P.; Chu, W.; Yu, M.; Yang, F.; Wu, Z.; Wu, J.; Shi, Y.. "Solution structure of human DESR1, a CSL zinc-binding protein."  Proteins 71, 514-518 (2008).
PubMed: 18214955

Assembly members:

Assembly members:
DESR1, polymer, 89 residues, 9512.521 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts317
15N chemical shifts76
1H chemical shifts535

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DESR11
2ZN2

Entities:

Entity 1, DESR1 89 residues - 9512.521 Da.

1   METALAVALPHEHISASPGLUVALGLUILE
2   GLUASPPHEGLNTYRASPGLUASPSERGLU
3   THRTYRPHETYRPROCYSPROCYSGLYASP
4   ASNPHESERILETHRLYSGLUASPLEUGLU
5   ASNGLYGLUASPVALALATHRCYSPROSER
6   CYSSERLEUILEILELYSVALILETYRASP
7   LYSASPGLNPHEVALSERGLYGLUTHRVAL
8   PROALAPROSERALAASNLYSGLULEUVAL
9   LYSLEUGLUHISHISHISHISHISHIS

Entity 2, ZN - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: entity_1, [U-99% 13C; U-99% 15N], 1.5 mM; TRIS 20 mM; sodium chloride 50 mM; beta-mercaptoethanol 14 mM; H2O 90%; D2O 10%

sample_2: entity_1, [U-99% 13C; U-99% 15N], 1.5 mM; TRIS 20 mM; sodium chloride 50 mM; beta-mercaptoethanol 14 mM; D2O 99.9%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMRPipe v2.2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3, Goddard - data analysis

CSI v1.0, David S. Wishart - data analysis

Molmol v2K.2, Koradi, Billeter and Wuthrich - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAE02507
EMBL CAH92222
GB AAH10181 AAI68674 ADZ15684 AIC53581 EAW64268
REF NP_001126299 NP_001247449 NP_996662 XP_002759684 XP_002814073
SP Q4R312 Q5R7N8 Q96FX2
AlphaFold Q4R312 Q5R7N8 Q96FX2

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