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 50465

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50465

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Title: 1H, 13C and 15N chemical shift assignments of the human Death-associated protein 1 (DAP-1)   PubMed: 33263927

Deposition date: 2020-09-08 Original release date: 2021-04-13

Authors: Voigt, Johanna; Jirschitzka, Jan; Hafner, Sabine; Ohlenschlager, Oliver; Bordusa, Frank; Wiedemann, Christoph

Citation: Wiedemann, Christoph; Voigt, Johanna; Jirschitzka, Jan; Hafner, Sabine; Ohlenschlager, Oliver; Bordusa, Frank. "Backbone and nearly complete side-chain chemical shift assignments of the human death-associated protein 1 (DAP1)"  Biomol. NMR Assignments 15, 91-97 (2021).

Assembly members:
entity_1, polymer, 122 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-His6-hDAP1

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MSSPPEGKLETKAGHPPAVK AGGMRIVQKHPHTGDTKEEK DKDDQEWESPSPPKPTVFIS GVIARGDKDFPPAAAQVAHQ KPHASMDKHPSPRTQHIQQP RK

Data sets:
Data typeCount
13C chemical shifts471
15N chemical shifts114
1H chemical shifts700

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DAP-11

Entities:

Entity 1, DAP-1 122 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METSERSERPROPROGLUGLYLYSLEUGLU
4   THRLYSALAGLYHISPROPROALAVALLYS
5   ALAGLYGLYMETARGILEVALGLNLYSHIS
6   PROHISTHRGLYASPTHRLYSGLUGLULYS
7   ASPLYSASPASPGLNGLUTRPGLUSERPRO
8   SERPROPROLYSPROTHRVALPHEILESER
9   GLYVALILEALAARGGLYASPLYSASPPHE
10   PROPROALAALAALAGLNVALALAHISGLN
11   LYSPROHISALASERMETASPLYSHISPRO
12   SERPROARGTHRGLNHISILEGLNGLNPRO
13   ARGLYS

Samples:

sample_1: human Death-associated protein 1, [U-99% 13C; U-99% 15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 150 mM; sodium azide 0.05%; H2O 90%; D2O, [U-99% 2H], 10%; DSS 2 mM

sample_conditions_1: ionic strength: 180 mM; pH: 6.5; pressure: 1 atm; temperature: 283.2 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 HNCAsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D CACOsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
3D HCACONsample_1isotropicsample_conditions_1
3D HCANsample_1isotropicsample_conditions_1
3D HACACONCAHsample_1isotropicsample_conditions_1
3D HANHsample_1isotropicsample_conditions_1
3D HACONHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

ANALYSIS v2.5 - chemical shift assignment

TOPSPIN v3.6.2 - collection, processing

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

Related Database Links:

UNP P51397
AlphaFold Q9BUC9

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