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 18954

Title: NMR structure of the GUCT domain from human DEAD box polypeptide 21

Deposition date: 2013-01-16 Original release date: 2013-01-28

Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the GUCT domain from human DEAD box polypeptide 21 (DDX21)"  Not known ., .-..

Assembly members:
entity, polymer, 95 residues, 10640.232 Da.

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

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

Entity Sequences (FASTA):
entity: GHISGATSVDQRSLINSNVG FVTMILQCSIEMPNISYAWK ELKEQLGEEIDSKVKGMVFL KGKLGVCFDVPTASVTEIQE KWHDSRRWQLSVATE

Data sets:
Data typeCount
13C chemical shifts307
15N chemical shifts101
1H chemical shifts658

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GUCT1

Entities:

Entity 1, GUCT 95 residues - 10640.232 Da.

1   GLYHISILESERGLYALATHRSERVALASP
2   GLNARGSERLEUILEASNSERASNVALGLY
3   PHEVALTHRMETILELEUGLNCYSSERILE
4   GLUMETPROASNILESERTYRALATRPLYS
5   GLULEULYSGLUGLNLEUGLYGLUGLUILE
6   ASPSERLYSVALLYSGLYMETVALPHELEU
7   LYSGLYLYSLEUGLYVALCYSPHEASPVAL
8   PROTHRALASERVALTHRGLUILEGLNGLU
9   LYSTRPHISASPSERARGARGTRPGLNLEU
10   SERVALALATHRGLU

Samples:

sample_1: GUCT, [U-99% 13C; U-99% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; D2O, [U-99% 2H], 95%; H2O 5%

sample_conditions_1: ionic strength: 0.798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
4D APSY HACANHsample_1isotropicsample_conditions_1
5D APSY HACACONHsample_1isotropicsample_conditions_1
5D APSY CBCACONHsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, G ntert P. - structure solution

TOPSPIN v3.1, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

j-UNIO, Herrmann, and Wuthrich - chemical shift assignment, peak picking, structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB93481 BAG37957 BAI45572
EMBL CAH18395
GB AAB02546 AAF78930 AAH08071 ABM84557 ABM87851
REF NP_001243839 NP_004719 XP_001110939 XP_002820927 XP_003258243
SP Q9NR30

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