BMRB Entry 18765

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18765

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Title:
Backbone and side-chain assignments of 1H, 15N and 13C chemical shifts of RNA recognition motif 1 (RRM1) of TAR DNA-binding protein (TDP-43)
Deposition date:
2012-10-07
Original release date:
2013-01-16
Authors:
Chang, Chung-ke; Chiang, Ming-hui; Toh, Elsie; Huang, Tai-huang
Citation:

Citation: Chang, Chung-ke; Chiang, Ming-hui; Toh, Elsie Khai-Woon; Chang, Chi-Fon; Huang, Tai-huang. "Molecular mechanism of oxidation-induced TDP-43 RRM1 aggregation and loss of function."  FEBS Lett. 587, 575-582 (2013).
PubMed: 23384725

Assembly members:

Assembly members:
RRM1, polymer, 103 residues, Formula weight is not available

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: pQE30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RRM1: MRGSHHHHHHGSQKTSDLIV LGLPWKTTEQDLKEYFSTFG EVLMVQVKKDLKTGHSKGFG FVRFTEYETQVKVMSQRHMI DGRWCDCKLPNSKQSQDEPL RSR

Data sets:
Data typeCount
13C chemical shifts415
15N chemical shifts99
1H chemical shifts642

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RRM11

Entities:

Entity 1, RRM1 103 residues - Formula weight is not available

Residues 1-12 represent a non-native affinity tag. The rest of the molecule corresponds to residues 101-191 in native TDP-43 protein.

1   METARGGLYSERHISHISHISHISHISHIS
2   GLYSERGLNLYSTHRSERASPLEUILEVAL
3   LEUGLYLEUPROTRPLYSTHRTHRGLUGLN
4   ASPLEULYSGLUTYRPHESERTHRPHEGLY
5   GLUVALLEUMETVALGLNVALLYSLYSASP
6   LEULYSTHRGLYHISSERLYSGLYPHEGLY
7   PHEVALARGPHETHRGLUTYRGLUTHRGLN
8   VALLYSVALMETSERGLNARGHISMETILE
9   ASPGLYARGTRPCYSASPCYSLYSLEUPRO
10   ASNSERLYSGLNSERGLNASPGLUPROLEU
11   ARGSERARG

Samples:

sample_1: RRM1, [U-100% 13C; U-100% 15N], 0.5 mM; HEPES 25 mM; sodium chloride 150 mM; DTT 1 mM; imidazole 50 mM

sample_conditions_1: pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C TROSY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

ANALYSIS v2.2, CCPN - chemical shift assignment, peak picking

xwinnmr v3.0, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAC27753 BAC32395 BAC38861 BAD96474 BAE21557
EMBL CAB43367 CAG38565 CAH92854 CAL37794
GB AAA70033 AAH12873 AAH25544 AAH27105 AAH27772
REF NP_001003898 NP_001003899 NP_001008545 NP_001008546 NP_001011979
SP Q13148 Q5R5W2 Q921F2
AlphaFold Q13148 Q5R5W2 Q921F2

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