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 51301

Title: Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein   PubMed: 35474152

Deposition date: 2022-02-04 Original release date: 2022-05-27

Authors: Obika, Kingsley Benjamin; Liebscher, Sandra; Jirscitzka, Jan; Ohlenschlager, Oliver; Bordusa, Frank; Wiedemann, Christoph

Citation: Wiedemann, Christoph; Obika, Kingsley Benjamin; Liebscher, Sandra; Jirschitzka, Jan; Ohlenschlager, Oliver; Bordusa, Frank. "Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein"  Biomol. NMR Assignments 16, 237-246 (2022).

Assembly members:
entity_1, polymer, 178 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MEPPEGAGTGEIVKEAEVPQ AALGVPAQGTGDNGHTPVEE EVGGIPVPAPGLLQVTERRQ PLSSVSSLEVHFDLLDLTEL TDMSDQELAEVFADSDDENL NTESPAGLHPLPRAGYLRSP SWTRTRAEQSHEKQPLGDPE RQATVLDTFLTVERPQED

Data sets:
Data typeCount
13C chemical shifts667
15N chemical shifts171
1H chemical shifts903

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human DBNDD11

Entities:

Entity 1, human DBNDD1 178 residues - Formula weight is not available

Purification tag N-terminal to natural sequence, purification tag numbered from -19-0.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METGLUPROPROGLUGLYALAGLYTHRGLY
4   GLUILEVALLYSGLUALAGLUVALPROGLN
5   ALAALALEUGLYVALPROALAGLNGLYTHR
6   GLYASPASNGLYHISTHRPROVALGLUGLU
7   GLUVALGLYGLYILEPROVALPROALAPRO
8   GLYLEULEUGLNVALTHRGLUARGARGGLN
9   PROLEUSERSERVALSERSERLEUGLUVAL
10   HISPHEASPLEULEUASPLEUTHRGLULEU
11   THRASPMETSERASPGLNGLULEUALAGLU
12   VALPHEALAASPSERASPASPGLUASNLEU
13   ASNTHRGLUSERPROALAGLYLEUHISPRO
14   LEUPROARGALAGLYTYRLEUARGSERPRO
15   SERTRPTHRARGTHRARGALAGLUGLNSER
16   HISGLULYSGLNPROLEUGLYASPPROGLU
17   ARGGLNALATHRVALLEUASPTHRPHELEU
18   THRVALGLUARGPROGLNGLUASP

Samples:

sample_1: human DBNDD1, [U-99% 13C; U-99% 15N], 300 uM; DSS 100 uM; sodium phosphate 10 mM; sodium chloride 150 mM

sample_2: human DBNDD1, [U-99% 13C; U-99% 15N], 300 uM; DSS 100 uM; sodium phosphate 10 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 0.16 M; pH: 6.5; pressure: 1 atm; temperature: 283.2 K

sample_conditions_2: ionic strength: 0.16 M; pH: 6.5; pressure: 1 atm; temperature: 293.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D CONsample_2isotropicsample_conditions_2
(H)CACOsample_2isotropicsample_conditions_2
(H)CBCACONsample_2isotropicsample_conditions_2
(H)CBCANCOsample_2isotropicsample_conditions_2

Software:

CcpNMR - chemical shift assignment

TOPSPIN v3.6.2 - collection, processing

NMRbox - data analysis

NMR spectrometers:

  • Bruker AVANCE III 700.5 MHz
  • Bruker AVANCE III 700 MHz

Related Database Links:

UNP Q9H9R9
AlphaFold Q9BW25

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